1jjv

<table><tr><td colspan='2'>[[1jjv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JJV OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JJV FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">YacE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=727 "Bacterium influenzae" Lehmann and Neumann 1896])</td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Dephospho-CoA_kinase Dephospho-CoA kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.24 2.7.1.24] </span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jjv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jjv OCA], [http://pdbe.org/1jjv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jjv RCSB], [http://www.ebi.ac.uk/pdbsum/1jjv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jjv ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/COAE_HAEIN COAE_HAEIN]] Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A (By similarity).

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== Publication Abstract from PubMed ==

Dephospho-coenzyme A kinase catalyzes the final step in CoA biosynthesis, the phosphorylation of the 3'-hydroxyl group of ribose using ATP as a phosphate donor. The protein from Haemophilus influenzae was cloned and expressed, and its crystal structure was determined at 2.0-A resolution in complex with ATP. The protein molecule consists of three domains: the canonical nucleotide-binding domain with a five-stranded parallel beta-sheet, the substrate-binding alpha-helical domain, and the lid domain formed by a pair of alpha-helices. The overall topology of the protein resembles the structures of nucleotide kinases. ATP binds in the P-loop in a manner observed in other kinases. The CoA-binding site is located at the interface of all three domains. The double-pocket structure of the substrate-binding site is unusual for nucleotide kinases. Amino acid residues implicated in substrate binding and catalysis have been identified. The structure analysis suggests large domain movements during the catalytic cycle.

Crystal structure of dephospho-coenzyme A kinase from Haemophilus influenzae.,Obmolova G, Teplyakov A, Bonander N, Eisenstein E, Howard AJ, Gilliland GL J Struct Biol. 2001 Nov;136(2):119-25. PMID:11886213<ref>PMID:11886213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jjv" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacterium influenzae lehmann and neumann 1896]]

[[Category: Dephospho-CoA kinase]]

[[Category: Bonander, N]]

[[Category: Eisenstein, E]]

[[Category: Gilliland, G L]]

[[Category: Howard, A J]]

[[Category: Obmolova, G]]

[[Category: S2F, Structure 2.Function Project]]

[[Category: Teplyakov, A]]

[[Category: Transferase]]